Mouse Prkcd Antibody (N-Term) Blocking Peptide Synthetic Peptide Catalog # Bp14629a
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10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 Mouse Prkcd Antibody (N-term) Blocking Peptide Synthetic peptide Catalog # BP14629a Specification Mouse Prkcd Antibody (N-term) Blocking Mouse Prkcd Antibody (N-term) Blocking Peptide Peptide - Background - Product Information This is calcium-independent, Primary Accession P28867 phospholipid-dependent, serine-and threonine-specific enzyme. PKC is activated by diacylglycerol which in turn phosphorylates a Mouse Prkcd Antibody (N-term) Blocking Peptide - Additional Information range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters. May play a role in Gene ID 18753 antigen-dependent control of B-cell function. Phosphorylates MUC1 in the C-terminal and Other Names regulates the interaction between MUC1 and Protein kinase C delta type, beta-catenin (By similarity). Tyrosine-protein kinase PRKCD, nPKC-delta, Protein kinase C delta type regulatory Mouse Prkcd Antibody (N-term) Blocking subunit, Protein kinase C delta type catalytic subunit, Sphingosine-dependent Peptide - References protein kinase-1, SDK1, Prkcd, Pkcd Ronda, A.C., et al. J. Steroid Biochem. Mol. Format Biol. 122(4):287-294(2010)Li, X., et al. J. Am. Peptides are lyophilized in a solid powder Soc. Nephrol. format. Peptides can be reconstituted in 21(7):1115-1124(2010)Romanova, L.Y., et al. J. solution using the appropriate buffer as Cell. Sci. 123 (PT 9), 1567-1577 (2010) :White, needed. M.C., et al. PLoS Genet. 6 (6), E1000984 (2010) :Niger, C., et al. BMC Biochem. 11, 14 (2010) : Storage Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. Precautions This product is for research use only. Not for use in diagnostic or therapeutic procedures. Mouse Prkcd Antibody (N-term) Blocking Peptide - Protein Information Name Prkcd {ECO:0000312|MGI:MGI:97598} Synonyms Pkcd Function Calcium-independent, phospholipid- and diacylglycerol (DAG)- dependent serine/threonine-protein kinase that plays Page 1/4 10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 contrasting roles in cell death and cell survival by functioning as a pro-apoptotic protein during DNA damage-induced apoptosis, but acting as an anti- apoptotic protein during cytokine receptor-initiated cell death, is involved in tumor suppression, is required for oxygen radical production by NADPH oxidase and acts as positive or negative regulator in platelet functional responses. Negatively regulates B cell proliferation and also has an important function in self-antigen induced B cell tolerance induction (PubMed:<a href="http: //www.uniprot.org/citations/11976686" target="_blank">11976686</a>, PubMed:<a href="http://www.uniprot.org/ci tations/11976687" target="_blank">11976687</a>). Upon DNA damage, activates the promoter of the death-promoting transcription factor BCLAF1/Btf to trigger BCLAF1-mediated p53/TP53 gene transcription and apoptosis. In response to oxidative stress, interact with and activate CHUK/IKKA in the nucleus, causing the phosphorylation of p53/TP53. In the case of ER stress or DNA damage- induced apoptosis, can form a complex with the tyrosine-protein kinase ABL1 which trigger apoptosis independently of p53/TP53. In cytosol can trigger apoptosis by activating MAPK11 or MAPK14, inhibiting AKT1 and decreasing the level of X-linked inhibitor of apoptosis protein (XIAP), whereas in nucleus induces apoptosis via the activation of MAPK8 or MAPK9. Upon ionizing radiation treatment, is required for the activation of the apoptosis regulators BAX and BAK, which trigger the mitochondrial cell death pathway. Can phosphorylate MCL1 and target it for degradation which is sufficient to trigger for BAX activation and apoptosis. Is required for the control of cell cycle progression both at G1/S and G2/M phases. Mediates phorbol 12-myristate 13-acetate (PMA)-induced inhibition of cell cycle progression at G1/S phase by up- regulating the CDK inhibitor CDKN1A/p21 and inhibiting the cyclin CCNA2 promoter activity. In response to UV irradiation can phosphorylate CDK1, which is important for the G2/M DNA damage checkpoint activation (PubMed:<a href="htt p://www.uniprot.org/citations/19917613" target="_blank">19917613</a>). Can protect glioma cells from the apoptosis induced by TNFSF10/TRAIL, probably by inducing increased phosphorylation and Page 2/4 10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 subsequent activation of AKT1. Can also act as tumor suppressor upon mitogenic stimulation with PMA or TPA (By similarity). In N-formyl- methionyl-leucyl-phenylalanine (fMLP)-treated cells, is required for NCF1 (p47-phox) phosphorylation and activation of NADPH oxidase activity, and regulates TNF-elicited superoxide anion production in neutrophils, by direct phosphorylation and activation of NCF1 or indirectly through MAPK1/3 (ERK1/2) signaling pathways (PubMed:<a href="http://www.uniprot.org/c itations/18025218" target="_blank">18025218</a>). Involved in antifungal immunity by mediating phosphorylation and activation of CARD9 downstream of C-type lectin receptors activation, promoting interaction between CARD9 and BCL10, followed by activation of NF-kappa-B and MAP kinase p38 pathways (PubMed:<a href="http://www.uniprot.org/c itations/22265677" target="_blank">22265677</a>). May also play a role in the regulation of NADPH oxidase activity in eosinophil after stimulation with IL5, leukotriene B4 or PMA. In collagen-induced platelet aggregation, acts a negative regulator of filopodia formation and actin polymerization by interacting with and negatively regulating VASP phosphorylation. Downstream of PAR1, PAR4 and CD36/GP4 receptors, regulates differentially platelet dense granule secretion; acts as a positive regulator in PAR-mediated granule secretion, whereas it negatively regulates CD36/GP4-mediated granule release. Phosphorylates MUC1 in the C-terminal and regulates the interaction between MUC1 and beta-catenin. The catalytic subunit phosphorylates 14-3-3 proteins (YWHAB, YWHAZ and YWHAH) in a sphingosine-dependent fashion (PubMed:<a href="http://www.uniprot.org/citations/9705 322" target="_blank">9705322</a>). Phosphorylates ELAVL1 in response to angiotensin-2 treatment (By similarity). Phosphorylates mitochondrial phospolipid scramblase 3 (PLSCR3), resulting in increased cardiolipin expression on the mitochondrial outer membrane which facilitates apoptosis (By similarity). Phosphorylates SMPD1 which induces SMPD1 secretion (By similarity). Cellular Location Cytoplasm Page 3/4 10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 {ECO:0000250|UniProtKB:Q05655}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q05655}. Nucleus {ECO:0000250|UniProtKB:Q05655}. Cell membrane {ECO:0000250|UniProtKB:Q05655}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q05655}. Mitochondrion {ECO:0000250|UniProtKB:Q05655}. Endomembrane system {ECO:0000250|UniProtKB:Q05655}. Note=Translocates to the mitochondria upon apoptotic stimulation. Upon activation, translocates to the plasma membrane followed by partial location to the endolysosomes {ECO:0000250|UniProtKB:Q05655} Tissue Location Isoform 1 is highly expressed in developing pro- and pre-B-cells and moderately in mature T-cells. Isoform 2 is highly expressed in testis and ovary and at a lower level in thymocytes, brain and kidney Mouse Prkcd Antibody (N-term) Blocking Peptide - Protocols Provided below are standard protocols that you may find useful for product applications. • Blocking Peptides Page 4/4 Powered by TCPDF (www.tcpdf.org).